The apyrase KlYnd1p of<i>Kluyveromyces lactis</i>affects glycosylation, secretion, and cell wall properties

Uccelletti, Daniela; Anticoli, Simona; Palleschi, Claudio

doi:10.1111/j.1567-1364.2007.00229.x

Cited by 7 publications

(7 citation statements)

References 27 publications

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“…In other fungal species, there also appear to be Golgi-localized apyrases, based on experimental evidence, as well as on sequence analyses that predict their cellular localization. Golgi-localized apyrases have been characterized in nonpathogenic and pathogenic fungi, where they play an important role in secretion and cell wall processes (Herrero et al, 2002;Lopez-Esparza et al, 2013;Uccelletti et al, 2007). However, there is also some evidence for surface-localized ecto-apyrase activity in human fungal pathogens (Collopy-Junior et al, 2006;Junior et al, 2005;Kiffer-Moreira et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Apyrase inhibitors enhance the ability of diverse fungicides to inhibit the growth of different plant‐pathogenic fungi

Tripathy

Weeraratne

Clark

et al. 2016

Molecular Plant Pathology

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A previous study has demonstrated that the treatment of Arabidopsis plants with chemical inhibitors of apyrase enzymes increases their sensitivity to herbicides. In this study, we found that the addition of the same or related apyrase inhibitors could potentiate the ability of different fungicides to inhibit the growth of five different pathogenic fungi in plate growth assays. The growth of all five fungi was partially inhibited by three commonly used fungicides: copper octanoate, myclobutanil and propiconazole. However, when these fungicides were individually tested in combination with any one of four different apyrase inhibitors (AI.1, AI.10, AI.13 or AI.15), their potency to inhibit the growth of five fungal pathogens was increased significantly relative to their application alone. The apyrase inhibitors were most effective in potentiating the ability of copper octanoate to inhibit fungal growth, and least effective in combination with propiconazole. Among the five pathogens assayed, that most sensitive to the fungicide-potentiating effects of the inhibitors was Sclerotinia sclerotiorum. Overall, among the 60 treatment combinations tested (five pathogens, four apyrase inhibitors, three fungicides), the addition of apyrase inhibitors increased significantly the sensitivity of fungi to the fungicide treatments in 53 of the combinations. Consistent with their predicted mode of action, inhibitors AI.1, AI.10 and AI.13 each increased the level of propiconazole retained in one of the fungi, suggesting that they could partially block the ability of efflux transporters to remove propiconazole from these fungi.

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Section: Introductionmentioning

confidence: 99%

Apyrase inhibitors enhance the ability of diverse fungicides to inhibit the growth of different plant‐pathogenic fungi

Tripathy

Weeraratne

Clark

et al. 2016

Molecular Plant Pathology

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“…For instance, it has been shown that apyrase Ynd1 can fulfil the absence of the GDA1 gene which codifies for this enzyme in Saccharomyces cerevisiae (Uccelletti et al 2007;Abeijon et al 1993;Gao et al 1999). In the same line, mutant gda1Δ cells of Schizosaccharomyces pombe and Kluyveromyces lactis are able to carry out the N-or O-glycosylation as apyrases SpYnd1p and KlYndp1 conduct this function in the absence of the GDA1 gene (D'Alessio et al 2003;LopezAvalos et al 2001).…”

Section: Ros Affect Gdpase/udpase Activity In Candida Speciesmentioning

confidence: 98%

“…A malfunction on any of the glycosylation pathways might cause an irreparable damage (Uccelletti et al 2007(Uccelletti et al , 2008Sánchez et al 2003;Lopez-Avalos et al 2001;Gao et al 1999). Protein glycosylation starts at the endoplasmic reticulum and ends in the Golgi apparatus where it requires nucleotide sugars that are produced in the cytosol in the form of nucleoside diphosphate (NDP)-sugar donors (Gao et al 1999;Uccelletti et al 2007). After transport and transfer of the sugars to the appropriate macromolecular acceptors in the lumen of these vesicles, released NDPs are substrates for NDPases, which convert them into the corresponding nucleoside monophosphates (NMPs) that exit the Golgi in a coupled equimolar exchange with cytosolic nucleotide sugars by antiport transport systems (Hirschberg and Snider 1987).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Changes in GDPase/UDPase enzymatic activity in response to oxidative stress in four Candida species

et al. 2015

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The terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. In addition, NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties. Interest of this laboratory has recently focused on the effect of reactive oxygen species (ROS) on enzymes involved in detoxification of these oxidants and on the metabolism of biomolecules such as lipids, nucleic acids, and proteins in human pathogenic Candida species. We therefore consider it important to extend these studies to determine how GDPase and UDPase are affected after exposure of cells to oxidants such as menadione, a superoxide (O2 (•-))-generator, and H2O2. Results indicate that activity of both enzymes decrease in response to these agents suggesting that ROS may also affect other critical cell functions such as protein glycosylation.

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“…Several genes, when overexpressed, enhance the release of heterologous proteins outside the cell. These helper genes code for proteins involved in the glycosylation pathway (37,38), in the oxidative folding machinery (19), in the UPR (2), in the ER-Golgi membrane trafficking and exocytosis (34).…”

Section: Discussionmentioning

confidence: 99%

SOD1, a New Kluyveromyces lactis Helper Gene for Heterologous Protein Secretion

Raimondi

Zanni

Talora

et al. 2008

Appl Environ Microbiol

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Bottlenecks in protein expression and secretion often limit the development of industrial processes. By manipulating chaperone and foldase levels, improvements in yeast secretion were found for a number of proteins. Recently, sustained endoplasmic reticulum stress, occurring due to recombinant protein production, was reported to cause oxidative stress in yeast. Saccharomyces cerevisiae cells are able to trigger an adaptive response to oxidative-stress conditions, resulting in the upregulation of both primary and secondary antioxidant defenses. SOD1 encodes for a superoxide dismutase that catalyzes the dismutation of superoxide anions (O 2 ؊ ) into oxygen and hydrogen peroxide. It is a Cu 2؉ /Zn 2؉ metalloenzyme and represents an important antioxidant defense in nearly all aerobic and aerotolerant organisms. We found that overexpression of the Kluyveromyces lactis SOD1 (KlSOD1) gene was able to increase the production of two different heterologous proteins, human serum albumin (HSA) and glucoamylase from Arxula adeninivorans. In addition, KlSOD1 overexpression led to a significant decrease in the amount of reactive oxygen species (ROS) that originated during protein production. The yield of HSA also increased when K. lactis cells were grown in the presence of the antioxidant agent ascorbic acid and decreased when cells were challenged with menadione, a ROS generator compound. Moreover, we observed that, in high-osmolarity medium, cells overexpressing KlSOD1 showed higher growth rates than control cells. Our results thus further support the notion that the production of some heterologous proteins may be improved by manipulating genes involved in general stress responses.

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The apyrase KlYnd1p ofKluyveromyces lactisaffects glycosylation, secretion, and cell wall properties

Cited by 7 publications

References 27 publications

Apyrase inhibitors enhance the ability of diverse fungicides to inhibit the growth of different plant‐pathogenic fungi

Apyrase inhibitors enhance the ability of diverse fungicides to inhibit the growth of different plant‐pathogenic fungi

Changes in GDPase/UDPase enzymatic activity in response to oxidative stress in four Candida species

SOD1, a New Kluyveromyces lactis Helper Gene for Heterologous Protein Secretion

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